Species | Clostridium beijerinckii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium beijerinckii | |||||||||||
CAZyme ID | MGYG000004667_01710 | |||||||||||
CAZy Family | GH50 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 22626; End: 24833 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH50 | 95 | 730 | 4.3e-160 | 0.9800918836140888 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam17992 | Agarase_CBM | 3.14e-07 | 61 | 224 | 17 | 178 | Agarase CBM like domain. This is the N-terminal CBM-like domain in exo-beta-agarase proteins (EC:3.2.1.81) found in the marine microbe Saccharophagus degradans. This enzyme catalyzes a critical step in the metabolism of agarose by S. degradans through cleaving agarose oligomers into neoagarobiose products that can be further processed into monomers. The CBM-like domain is structurally very similar to some CBM families. A loop in the CBM-like domain is involved in forming the roof of the active site channel. The contribution of the CBM-like domain to formation of the active site of the enzyme supports a role in substrate recognition explaining the exo-mode of beta-agarase action. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUI25447.1 | 0.0 | 28 | 734 | 26 | 736 |
QCT03652.1 | 5.03e-200 | 39 | 734 | 28 | 723 |
AVV48109.1 | 8.47e-199 | 34 | 734 | 15 | 715 |
AKV62624.1 | 3.04e-198 | 33 | 734 | 25 | 723 |
QTH40776.1 | 3.04e-198 | 33 | 734 | 25 | 723 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
4BQ2_A | 3.07e-129 | 163 | 730 | 137 | 743 | Structuralanalysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_C Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_D Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_A Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_C Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_D Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40] |
4BQ4_A | 8.54e-129 | 163 | 730 | 137 | 743 | Structuralanalysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ4_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ5_A Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ5_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40] |
6XJ9_A | 1.79e-128 | 56 | 734 | 44 | 763 | Structureof PfGH50B [Pseudoalteromonas fuliginea],6XJ9_B Structure of PfGH50B [Pseudoalteromonas fuliginea] |
5Z6P_A | 5.39e-127 | 86 | 734 | 76 | 763 | Thecrystal structure of an agarase, AgWH50C [Agarivorans gilvus],5Z6P_B The crystal structure of an agarase, AgWH50C [Agarivorans gilvus] |
5T3B_A | 2.27e-18 | 274 | 732 | 84 | 475 | ChainA, Glycoside Hydrolase [Phocaeicola plebeius],5T3B_B Chain B, Glycoside Hydrolase [Phocaeicola plebeius] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P48840 | 3.99e-131 | 29 | 734 | 224 | 953 | Beta-agarase B OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaB PE=3 SV=1 |
P48839 | 5.14e-103 | 42 | 730 | 206 | 913 | Beta-agarase A OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000249 | 0.999091 | 0.000174 | 0.000179 | 0.000146 | 0.000131 |
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